Schmidt, A <br/><br/>
Structures of three inhibitor complexes provide insight into the reaction mechanism of the human methylenetetrahydrofolate dehydrogenase/cyclohydrolase.  [electronic resource] 

 -  Biochemistry  May 2000 
 - 6325-35 p.  digital 
<br/><br/> Publication Type: Journal Article 
<br/><br/><label>ISSN: </label>0006-2960 
<br/><br/><label>Standard No.: </label>10.1021/bi992734y  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Amino Acid Sequence<br/>Aminohydrolases--antagonists & inhibitors<br/>Animals<br/>Binding Sites<br/>Crystallography, X-Ray<br/>Drosophila<br/>Escherichia coli--enzymology<br/>Folic Acid Antagonists--chemistry<br/>Humans<br/>Methylenetetrahydrofolate Dehydrogenase (NADP)--antagonists & inhibitors<br/>Mice<br/>Models, Molecular<br/>Molecular Sequence Data<br/>Multienzyme Complexes--antagonists & inhibitors<br/>Mutagenesis, Site-Directed<br/>NADP--metabolism<br/>Protein Conformation<br/>Rats<br/>Recombinant Proteins--antagonists & inhibitors<br/>Sequence Alignment<br/>Sequence Homology, Amino Acid<br/>Structure-Activity Relationship<br/>Tetrahydrofolates--chemistry